IED Industry Enzyme Database

Detail Information for IndEnz0001000598
IED ID IndEnz0001000598
Enzyme Type ID amylase000598
Protein Name Alpha-amylase
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
Gene Name amyS
Organism Geobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus)
Enzyme Sequence MLTFHRIIRKGWMFLLAFLLTALLFCPTGQPAKAAAPFNGTMMQYFEWYLPDDGTLWTKVANEANNLSSLGITALWLPPAYKGTSRSDVGYGVYDLYDLGEFNQKGAVRTKYGTKAQYLQAIQAAHAAGMQVYADVVFDHKGGADGTEWVDAVEVNPSDRNQEISGTYQIQAWTKFDFPGRGNTYSSFKWRWYHFDGVDWDESRKLSRIYKFRGIGKAWDWEVDTENGNYDYLMYADLDMDHPEVVTELKSWGKWYVNTTNIDGFRLDAVKHIKFSFFPDWLSDVRSQTGKPLFTVGEYWSYDINKLHNYIMKTNGTMSLFDAPLHNKFYTASKSGGTFDMRTLMTNTLMKDQPTLAVTFVDNHDTEPGQALQSWVDPWFKPLAYAFILTRQEGYPCVFYGDYYGIPQYNIPSLKSKIDPLLIARRDYAYGTQHDYLDHSDIIGWTREGVTEKPGSGLAALITDGPGGSKWMYVGKQHAGKVFYDLTGNRSDTVTINSDGWGEFKVNGGSVSVWVPRKTTVSTIAWSITTRPWTDEFVRWTEPRLVAWP
Enzyme Length 549
Uniprot Accession Number P06279
Absorption
Active Site ACT_SITE 268; /note=Nucleophile; ACT_SITE 298; /note=Proton donor
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:2999073};
DNA Binding
EC Number 3.2.1.1
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (27); Chain (1); Helix (16); Metal binding (18); Sequence conflict (27); Signal peptide (1); Site (1); Turn (7)
Keywords 3D-structure;Calcium;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2999073, ECO:0000269|Ref.4}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..34; /evidence="ECO:0000269|PubMed:2999073, ECO:0000269|PubMed:3924897"
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1HVX; 4UZU;
Mapped Pubmed ID 25615972;
Motif
Gene Encoded By
Mass 62,671
Kinetics
Metal Binding METAL 139; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 196; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 196; /note="Sodium"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 218; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 220; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 220; /note="Sodium"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 231; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 231; /note="Sodium"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 237; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 237; /note="Sodium"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 238; /note="Sodium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 239; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 272; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 337; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 339; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 440; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 441; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"; METAL 464; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:11226887, ECO:0007744|PDB:1HVX"
Rhea ID
Cross Reference Brenda 3.2.1.1;